3k8m Summary

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Crystal structure of SusG with acarbose

The structure was published by Koropatkin, N.M. and Smith, T.J., in 2010 in a paper entitled "SusG: A Unique Cell-Membrane-Associated alpha-Amylase from a Prominent Human Gut Symbiont Targets Complex Starch Molecules." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 2009.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of Alpha-amylase, susG.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Alpha-amylase, susG Q8A1G3 (24-692) (SUSG_BACTN)search Bacteroides thetaiotaomicron VPI-5482search 100% 669 97%
B Alpha-amylase, susG Q8A1G3 (24-692) (SUSG_BACTN)search Bacteroides thetaiotaomicron VPI-5482search 100% 669 97%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q8A1G3 (24 - 692) Alpha-amylase, susG Bacteroides thetaiotaomicron

Chain Sequence family (Pfam)
A, B (Q8A1G3) PF00128: Alpha amylase, catalytic domainsearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B (Q8A1G3) catalytic activitysearch cation bindingsearch alpha-amylase activitysearch hydrolase activity, acting on glycosyl bondssearch magnesium ion bindingsearch metal ion bindingsearch calcium ion bindingsearch starch bindingsearch hydrolase activitysearch carbohydrate metabolic processsearch polysaccharide catabolic processsearch starch catabolic processsearch metabolic processsearch membranesearch cell outer membranesearch outer membranesearch

Chain InterPro annotation
A, B Glycosyl hydrolase, family 13, catalytic domainsearch Glycosyl hydrolase, family 13, subfamily, catalytic domainsearch Glycosyl hydrolase, family 13, all-betasearch Glycoside hydrolase, catalytic domainsearch Glycoside hydrolase, family 13search Glycoside hydrolase, superfamilysearch